ID   Y4FR_SINFN              Reviewed;         546 AA.
AC   P55456;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase NGR_a03640;
DE            EC=2.3.2.-;
DE   AltName: Full=Probable E3 ubiquitin-protein transferase NGR_a03640 {ECO:0000305};
GN   OrderedLocusNames=NGR_a03640; ORFNames=y4fR;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. This protein is an E3
CC       ubiquitin ligase that interferes with host's ubiquitination pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Secreted via type III secretion system (TTSS), and
CC       delivered into the host cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: The LRR (leucine-rich repeat) domain forms a slightly curved
CC       solenoid and may mediate interaction with target proteins.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating
CC       enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC       {ECO:0000305}.
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DR   EMBL; U00090; AAB91674.1; -; Genomic_DNA.
DR   RefSeq; NP_443862.1; NC_000914.2.
DR   RefSeq; WP_010875377.1; NC_000914.2.
DR   AlphaFoldDB; P55456; -.
DR   SMR; P55456; -.
DR   STRING; 394.NGR_a03640; -.
DR   iPTMnet; P55456; -.
DR   EnsemblBacteria; AAB91674; AAB91674; NGR_a03640.
DR   KEGG; rhi:NGR_a03640; -.
DR   PATRIC; fig|394.7.peg.371; -.
DR   eggNOG; COG4886; Bacteria.
DR   HOGENOM; CLU_018533_2_0_5; -.
DR   OMA; IKGETME; -.
DR   OrthoDB; 259035at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR029487; NEL_dom.
DR   Pfam; PF14496; NEL; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Leucine-rich repeat; Plasmid; Reference proteome; Repeat;
KW   Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..546
FT                   /note="Probable E3 ubiquitin-protein ligase NGR_a03640"
FT                   /id="PRO_0000200841"
FT   REPEAT          104..125
FT                   /note="LRR 1"
FT   REPEAT          126..144
FT                   /note="LRR 2"
FT   REPEAT          145..166
FT                   /note="LRR 3"
FT   REPEAT          167..186
FT                   /note="LRR 4"
FT   REPEAT          187..208
FT                   /note="LRR 5"
FT   REGION          1..248
FT                   /note="Interaction with target proteins"
FT                   /evidence="ECO:0000250"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..256
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          257..546
FT                   /note="E3 ubiquitin-protein ligase catalytic domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        40..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        338
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  60460 MW;  8F6159EDC6ACD409 CRC64;
     MNVQRPGLAV GPLFENPESE SSEPGSPAAA ARWVEASTEA EASAASSSQG QIVAAPTAEE
     RPWEGRPQEA VSRTRAWREA GDVDEPLDLS FLSLTPLSIP LVSGLRRLNV NNNQLGDLPD
     TLPGTLLELE ASENRLTRLP DLPAGLQRLN VENNRLTNLP EPLPAALEWL GAGYNQLTRL
     PEMIPPELIW LGARNNQLTS VPESLLTQLG QWSSIDLENN PLPHGVQTNL VTAMHAAGYA
     GPQIFLPMGP VELARRPLHE VVADWLEGDL ETVAAWRGFA NEQGARDYAH FLDRLRTTVN
     YGNDAFRQAV AIGLRQAVAR PQLRAQYFEQ ASGASDSCED RITLTWNGMQ TALLIADVED
     GVYDGSLHQL LQHGRVMFRL EALDGIARET VNSLRRTDPD ADIDEIEVYL AYQTQLRDTL
     ELRHVAPDMR FLNVSHVTEE DVARAASSVR ELEARGFGEY VATRWQPWER VMRRIAPASH
     AAMQEQLIEA MGEEFRSRLD EKLAEHGLTG DADAERVFGA EILNDIARRI KGETMEKVLR
     GRGLEL